Difference between revisions of "YBR082C"
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− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000286 YBR082C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''UBC4 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''UBC4 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr II: | + | |nowrap| Chr II:407169..406628 |
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+ | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000286 | ||
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− | '''Description of | + | '''Description of YBR082C:''' Ubiquitin-conjugating enzyme (E2), mediates degradation of abnormal or excess proteins, including calmodulin and histone H3; interacts with many SCF ubiquitin protein ligases; component of the cellular stress response<ref name='S000075480'>Kus BM, et al. (2004) Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54(3):455-67 {{SGDpaper|S000075480}} PMID 14747994</ref><ref name='S000042559'>Parag HA, et al. (1993) Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae. FEBS Lett 325(3):242-6 {{SGDpaper|S000042559}} PMID 8391479</ref><ref name='S000042741'>Seufert W and Jentsch S (1990) Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J 9(2):543-50 {{SGDpaper|S000042741}} PMID 2154373</ref><ref name='S000052341'>Seufert W and Jentsch S (1991) Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biol Hung 42(1-3):27-37 {{SGDpaper|S000052341}} PMID 1844315</ref><ref name='S000130860'>Singh RK, et al. (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33 |
− | {{SGDpaper| | + | {{SGDpaper|S000130860}} PMID 19578373</ref> |
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==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
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+ | <!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation --> | ||
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+ | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
+ | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
+ | J Biol Chem 278(5):3265-74</ref> | ||
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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
Systematic name | YBR082C |
Gene name | UBC4 |
Aliases | |
Feature type | ORF, Verified |
Coordinates | Chr II:407169..406628 |
Primary SGDID | S000000286 |
Description of YBR082C: Ubiquitin-conjugating enzyme (E2), mediates degradation of abnormal or excess proteins, including calmodulin and histone H3; interacts with many SCF ubiquitin protein ligases; component of the cellular stress response[1][2][3][4][5]
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References
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- ↑ Kus BM, et al. (2004) Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54(3):455-67 SGD PMID 14747994
- ↑ Parag HA, et al. (1993) Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae. FEBS Lett 325(3):242-6 SGD PMID 8391479
- ↑ Seufert W and Jentsch S (1990) Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J 9(2):543-50 SGD PMID 2154373
- ↑ Seufert W and Jentsch S (1991) Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biol Hung 42(1-3):27-37 SGD PMID 1844315
- ↑ Singh RK, et al. (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33 SGD PMID 19578373
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